Evidence map›Paper›PMID 25958131›Full record

ArticleJournal of virological methods2015

Using proximity biotinylation to detect herpesvirus entry glycoprotein interactions: Limitations for integral membrane glycoproteins.

Michelle Lajko, Alexander F Haddad, Carolyn A Robinson, Sarah A Connolly

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of virological methods, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.6field-weighted citation impact, top 34% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Michelle LajkoDePaul University, Department of Biological Sciences, Chicago, IL, USA.
Alexander F HaddadDePaul University, Department of Health Sciences, Chicago, IL, USA.
Carolyn A RobinsonDePaul University, Department of Health Sciences, Chicago, IL, USA.
Sarah A ConnollyDePaul University, Department of Biological Sciences, Chicago, IL, USA; DePaul University, Department of Health Sciences, Chicago, IL, USA. Electronic address: sconnol6@depaul.edu.
DePaul University · US

Funding

HERPESVIRUS GENE EXPRESSION IN TRANSFORMED CELLSR01CA021776 · NCI · UNIVERSITY OF CHICAGO · PI LONGNECKER, RICHARD M · 1985 to 2017
$4.2M
HERPESVIRUS GENE EXPRESSION IN TRANSFORMED CELLSR37CA021776 · NCI · UNIVERSITY OF CHICAGO · PI SPEAR, PATRICIA G · 1987 to 1994
–
NCI NIH HHS CA021776NCI NIH HHS R01 CA021776
6 · The paper itself

Abstract

Herpesvirus entry into cells requires coordinated interactions among several viral transmembrane glycoproteins. Viral glycoproteins bind to receptors and interact with other glycoproteins to trigger virus-cell membrane fusion. Details of these glycoprotein interactions are not well understood because they are likely transient and/or low affinity. Proximity biotinylation is a promising protein-protein interaction assay that can capture transient interactions in live cells. One protein is linked to a biotin ligase and a second protein is linked to a short specific acceptor peptide (AP). If the two proteins interact, the ligase will biotinylate the AP, without requiring a sustained interaction. To examine herpesvirus glycoprotein interactions, the ligase and AP were linked to herpes simplex virus 1 (HSV1) gD and Epstein Barr virus (EBV) gB. Interactions between monomers of these oligomeric proteins (homotypic interactions) served as positive controls to demonstrate assay sensitivity. Heterotypic combinations served as negative controls to determine assay specificity, since HSV1 gD and EBV gB do not interact functionally. Positive controls showed strong biotinylation, indicating that viral glycoprotein proximity can be detected. Unexpectedly, the negative controls also showed biotinylation. These results demonstrate the special circumstances that must be considered when examining interactions among glycosylated proteins that are constrained within a membrane.

Indexed as

Host-Pathogen InteractionsVirus InternalizationAnimalsBiotinylationCHO CellsCricetulusHerpesvirus 1, HumanHerpesvirus 4, HumanMembrane GlycoproteinsProtein BindingProtein Interaction MappingStaining and LabelingVirologyMembrane GlycoproteinsHerpesvirusProtein–protein interactionsProximity biotinylationVirus entry

Identifiers

PMID25958131
PMCPMC4469388
OpenAlexW305765393

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.